Evidence map›Paper›PMID 42561060›Full record

ArticleScience (New York, N.Y.)2026

A molecular switch for coordinating kinesin and dynein transport of mitochondrial cargo.

Christina Gladkova, Maria G Paez-Segala, William P Grant, Mark Kittisopikul, Samuel A Myers, Yuxiao Wang, Ronald D Vale

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Christina GladkovaJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA, USA.ORCID 0009-0001-6280-5029
Maria G Paez-SegalaJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA, USA.ORCID 0000-0002-5699-6826
William P GrantShrike Research, New York, NY, USA.ORCID 0000-0001-9309-7937
Mark KittisopikulJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA, USA.ORCID 0000-0002-9558-6248
Samuel A MyersLa Jolla Institute for Immunology, La Jolla, CA, USA.
Yuxiao WangDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA, USA.
Ronald D ValeJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA, USA.ORCID 0000-0003-3460-2758

Funding

Elucidating the signaling and protein interaction networks of the O-GlcNAc transferase during embryonic stem cell state transitionsR35GM147554 · NIGMS · LA JOLLA INSTITUTE FOR IMMUNOLOGY · PI Samuel Anthony Myers · 2022 to 2026
$2.4M
Howard Hughes Medical InstituteNIGMS NIH HHS R35 GM147554
6 · The paper itself

Abstract

The cellular distribution of mitochondria in response to stress and local energy needs is governed by the relative activities of the microtubule-based molecular motors kinesin and dynein. The mechanism for switching between these two opposite-polarity microtubule motors remains unknown. In this study, we coupled a cellular synthetic cargo transport assay with AlphaFold2-guided mutagenesis to identify a regulatory helix in the mitochondrial adaptor protein [trafficking kinesin-binding protein (TRAK)] that mediates switching between kinesin- and dynein-driven transport. Differences in the helix sequence explained why two near-identical TRAK isoforms transported mitochondria in predominantly opposite directions. Phosphorylation of the regulatory helix by stress-activated kinases caused the activation of dynein and dissociation of kinesin. Our results reveal a molecular mechanism for coordinating the directional transport of mitochondria in response to intracellular signals.

Indexed as

Adaptor Proteins, Vesicular TransportDyneinsIntracellular Signaling Peptides and ProteinsKinesinsMitochondriaMitochondrial ProteinsNerve Tissue ProteinsBiological TransportCell LineHumansMicrotubulesPhosphorylationProtein IsoformsProtein Structure, SecondaryAdaptor Proteins, Vesicular TransportDyneinsIntracellular Signaling Peptides and ProteinsKinesinsMitochondrial ProteinsNerve Tissue ProteinsProtein IsoformsTRAK1 protein, humanTRAK2 protein, human

Identifiers

PMID42561060
PMCPMC13545989

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.